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Identification and Functional Analysis of Proteins Interacting with Streptomyces coelicolor RNase ES  

Kim, Jong-Myung (Department of Life Science, Chung-Ang University)
Song, Woo-Seok (Department of Life Science, Chung-Ang University)
Kim, Hyun-Lee (Department of Life Science, Chung-Ang University)
Go, Ha-Young (Department of Life Science, Chung-Ang University)
Lee, Kang-Seok (Department of Life Science, Chung-Ang University)
Publication Information
Korean Journal of Microbiology / v.43, no.1, 2007 , pp. 72-75 More about this Journal
Abstract
Using co-immunoprecipitation, we identified proteins interacting with Streptomyces coelicolor RNase ES, an ortholog of Escherichia coli RNase E that plays a major role in RNA decay and processing. Polyphosphate kinase and a homolog of exoribonuclease polynucleotide phosphorylase, guanosine pentaphosphate synthetase I that use inorganic phophate were co-precipitated with RNase E, indicating a possibility of S. coelicolor RNase ES to form a multiprotein complex called degradosome, which has been shown to be formed by RNase E in E. coli. Polynucleotide phophorylase proteins from these two phylogenetically distantly related bacteria species showed similar RNA cleavage action in vitro. These results imply the ability of RNase ES to form a multiprotein complex that has structurally and functionally similar to that of E. coli degradosome.
Keywords
degradosome; polynucleotide phosphorylase; polyphosphate kinase; RNase ES; S. coelicolor;
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